Evidence map›Paper›PMID 31703473›Full record

ReviewBiomolecules2019

Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis.

Michael Prattes, Yu-Hua Lo, Helmut Bergler, Robin E Stanley

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Neuronal processes contain the essential components for the late steps of ribosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Ribosome biogenesis and function in development and disease.Development (Cambridge, England) · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Polysome Profiling without Gradient Makers or Fractionation Systems.Journal of visualized experiments : JoVE · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Michael PrattesInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/EG, Graz A-8010, Austria.
Yu-Hua LoSignal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive, Research Triangle Park, Durham, NC 27709, USA.
Helmut BerglerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/EG, Graz A-8010, Austria.
Robin E StanleySignal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive, Research Triangle Park, Durham, NC 27709, USA.
National Institutes of Health · USUniversity of Graz · AT

Funding

Structure and Function of RNA Processing MachinesZIAES103247 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI STANLEY, ROBIN · 2015 to 2025
$22.9M
Austrian Science Fund FWF P 29451Austrian Science Fund FWF P 32536NIEHS NIH HHS ZIA ES103247
6 · The paper itself

Abstract

AAA-ATPases are molecular engines evolutionarily optimized for the remodeling of proteins and macromolecular assemblies. Three AAA-ATPases are currently known to be involved in the remodeling of the eukaryotic ribosome, a megadalton range ribonucleoprotein complex responsible for the translation of mRNAs into proteins. The correct assembly of the ribosome is performed by a plethora of additional and transiently acting pre-ribosome maturation factors that act in a timely and spatially orchestrated manner. Minimal disorder of the assembly cascade prohibits the formation of functional ribosomes and results in defects in proliferation and growth. Rix7, Rea1, and Drg1, which are well conserved across eukaryotes, are involved in different maturation steps of pre-60S ribosomal particles. These AAA-ATPases provide energy for the efficient removal of specific assembly factors from pre-60S particles after they have fulfilled their function in the maturation cascade. Recent structural and functional insights have provided the first glimpse into the molecular mechanism of target recognition and remodeling by Rix7, Rea1, and Drg1. Here we summarize current knowledge on the AAA-ATPases involved in eukaryotic ribosome biogenesis. We highlight the latest insights into their mechanism of mechano-chemical complex remodeling driven by advanced cryo-EM structures and the use of highly specific AAA inhibitors.

Indexed as

Adenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesEnergy MetabolismNuclear ProteinsRibosomal ProteinsRibosomesSaccharomyces cerevisiaeAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesNuclear ProteinsRibosomal ProteinsAAA-ATPasescryo-EMDrg1/SPATA5Rea1/Mdn1ribosome biogenesisRix7/NVL2small molecular weight inhibitorssubstrate processing

Identifiers

PMID31703473
PMCPMC6920918
OpenAlexW2988833431

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.